Q5SH52 (Q5SH52_THET8) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
GTP cyclohydrolase 1 HAMAP MF_00223
EC=3.5.4.16 HAMAP MF_00223

Alternative name(s):
GTP cyclohydrolase I HAMAP MF_00223

Gene names

Name:	folE HAMAP MF_00223
Ordered Locus Names:	TTHA1878

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP MF_00223 SAAS SAAS001474
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP MF_00223 SAAS SAAS001474
Subunit structure	Homopolymer By similarity. HAMAP MF_00223
Sequence similarities	Belongs to the GTP cyclohydrolase I family. HAMAP MF_00223

Ontologies

Keywords
Biological process	One-carbon metabolism HAMAP MF_00223
Ligand	GTP-binding HAMAP MF_00223 Metal-binding HAMAP MF_00223 SAAS SAAS001474 PDB 1WM9 PDB 1WUQ PDB 1WUR Nucleotide-binding Zinc HAMAP MF_00223 SAAS SAAS001474 PDB 1WM9 PDB 1WUQ PDB 1WUR
Molecular function	Hydrolase HAMAP MF_00223 SAAS SAAS001474 EMBL BAD71701.1
Technical term	3D-structure PDB 1WM9 PDB 1WUQ PDB 1WUR Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	108	1	Zinc PDB 1WM9 PDB 1WUQ PDB 1WUR
	Metal binding	108	1	Zinc By similarity HAMAP MF_00223
	Metal binding	111	1	Zinc By similarity HAMAP MF_00223
	Metal binding	111	1	Zinc; via pros nitrogen PDB 1WM9 PDB 1WUQ PDB 1WUR
	Metal binding	179	1	Zinc PDB 1WM9 PDB 1WUQ PDB 1WUR
	Metal binding	179	1	Zinc By similarity HAMAP MF_00223

Sequences

	Sequence		Length	Mass (Da)
	Q5SH52 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 81B31AAFD1709A71	FASTA	220	24,539
	10 20 30 40 50 60 MSPGPQSGGQ ERGSMERKMV ELEDTGLTFA TEVDLERLQA LAAEWLQVIG EDPGREGLLK 70 80 90 100 110 120 TPERVAKAWA FLTRGYRQRL EEVVGGAVFP AEGSEMVVVK GVEFYSMCEH HLLPFFGKVH 130 140 150 160 170 180 IGYIPDGKIL GLSKFARIVD MFARRLQVQE RLAVQIAEAI QEVLEPQGVG VVVEGVHLCM 190 200 210 220 MMRGVEKQHS RTVTSAMLGV FRENQKTREE FLSHLRDGTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative." Tanaka Y., Nakagawa N., Kuramitsu S., Yokoyama S., Masui R. J. Biochem. 138:263-275(2005) [PubMed: 16169877] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD71701.1.

RefSeq

YP_145144.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WM9	X-ray	2.20	A/B/C/D/E	1-220	[»]
1WUQ	X-ray	2.00	A/B/C/D/E	1-220	[»]
1WUR	X-ray	1.82	A/B/C/D/E	1-220	[»]

ProteinModelPortal

Q5SH52.

SMR

Q5SH52. Positions 32-216.

ModBase

Search...

Protein-protein interaction databases

STRING

Q5SH52.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3168138.

GenomeReviews

Gene locus TTHA1878 in contig AP008226_GR.

KEGG

ttj:TTHA1878.

NMPDR

fig|300852.3.peg.1421.

PATRIC

23958717. VBITheThe93045_1845.

Phylogenomic databases

eggNOG

COG0302.

HOGENOM

HBG370191.

OMA

KQIATAM.

PhylomeDB

Q5SH52.

ProtClustDB

PRK09347.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA1878-MONOMER.

Family and domain databases

HAMAP

MF_00223. FolE.
[Tree]

InterPro

IPR001474. GTP_CycHdrlase_I.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
IPR018234. GTP_CycHdrlase_I_CS.
[Graphical view]

KO

K01495.

PANTHER

PTHR11109. GTP_cyclohydro_I. 1 hit.

Pfam

PF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00063. FolE. 1 hit.

PROSITE

PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q5SH52_THET8

Accession

Primary (citable) accession number: Q5SH52

Entry history

Integrated into UniProtKB/TrEMBL:	December 21, 2004
Last sequence update:	December 21, 2004
Last modified:	December 14, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)